BMRB Entry 25989

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25989

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Title:
1H, 13C, and 15N Chemical Shift Assignments of HAdV E1A243 (E1A 12S)
Deposition date:
2016-03-11
Original release date:
2017-09-25
Authors:
Hosek, Tomas; Calcada, Eduardo; Salvi, Michele; Pagani, Talita; Nogueira, Marcela; Felli, Isabella; Pierattelli, Roberta
Citation:

Citation: Hosek, Tomas; Calcada, Eduardo; Nogueira, Marcela; Salvi, Michele; Pagani, Talita; Felli, Isabella; Pierattelli, Roberta. "Structural and Dynamic Characterization of the Molecular Hub Early Region 1A (E1A) from Human Adenovirus"  Chemistry 22, 13010-13013 (2016).
PubMed: 27490777

Assembly members:

Assembly members:
E1A-12S, polymer, 243 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human adenovirus 2   Taxonomy ID: 10515   Superkingdom: Viruses   Kingdom: not available   Genus/species: Mastadenovirus Human mastadenovirus C

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETG-20A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
E1A-12S: MRHIICHGGVITEEMAASLL DQLIEEVLADNLPPPSHFEP PTLHELYDLDVTAPEDPNEE AVSQIFPESVMLAVQEGIDL FTFPPAPGSPEPPHLSRQPE QPEQRALGPVSMPNLVPEVI DLTCHEAGFPPSDDEDEEGP VSEPEPEPEPEPEPARPTRR PKLVPAILRRPTSPVSRECN SSTDSCDSGPSNTPPEIHPV VPLCPIKPVAVRVGGRRQAV ECIEDLLNESGQPLDLSCKR PRP

Data sets:
Data typeCount
13C chemical shifts673
15N chemical shifts222
1H chemical shifts763

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1E1A-12S monomer1

Entities:

Entity 1, E1A-12S monomer 243 residues - Formula weight is not available

1   METARGHISILEILECYSHISGLYGLYVAL
2   ILETHRGLUGLUMETALAALASERLEULEU
3   ASPGLNLEUILEGLUGLUVALLEUALAASP
4   ASNLEUPROPROPROSERHISPHEGLUPRO
5   PROTHRLEUHISGLULEUTYRASPLEUASP
6   VALTHRALAPROGLUASPPROASNGLUGLU
7   ALAVALSERGLNILEPHEPROGLUSERVAL
8   METLEUALAVALGLNGLUGLYILEASPLEU
9   PHETHRPHEPROPROALAPROGLYSERPRO
10   GLUPROPROHISLEUSERARGGLNPROGLU
11   GLNPROGLUGLNARGALALEUGLYPROVAL
12   SERMETPROASNLEUVALPROGLUVALILE
13   ASPLEUTHRCYSHISGLUALAGLYPHEPRO
14   PROSERASPASPGLUASPGLUGLUGLYPRO
15   VALSERGLUPROGLUPROGLUPROGLUPRO
16   GLUPROGLUPROALAARGPROTHRARGARG
17   PROLYSLEUVALPROALAILELEUARGARG
18   PROTHRSERPROVALSERARGGLUCYSASN
19   SERSERTHRASPSERCYSASPSERGLYPRO
20   SERASNTHRPROPROGLUILEHISPROVAL
21   VALPROLEUCYSPROILELYSPROVALALA
22   VALARGVALGLYGLYARGARGGLNALAVAL
23   GLUCYSILEGLUASPLEULEUASNGLUSER
24   GLYGLNPROLEUASPLEUSERCYSLYSARG
25   PROARGPRO

Samples:

sample_1: E1A-12S, [U-95% 13C; U-95% 15N], 0.5 mM; HEPES 10 mM; potassium chloride 50 mM; DTT 10 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: E1A-12S, [U-95% 13C; U-95% 15N], 0.5 mM; HEPES 10 mM; potassium chloride 50 mM; DTT 10 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D CON-IPAPsample_1isotropicsample_conditions_1
4D HCBCACON-IPAPsample_1isotropicsample_conditions_1
4D HCBCANCO-IPAPsample_1isotropicsample_conditions_1
4D HCACONCACON- IPAPsample_1isotropicsample_conditions_1
4D HNCONCACON-IPAPsample_1isotropicsample_conditions_1
2D 1H-15N BEST-TROSYsample_2isotropicsample_conditions_1
3D BEST-TROSY HNCOsample_2isotropicsample_conditions_1
3D BEST-TROSY HNCACOsample_2isotropicsample_conditions_1
3D BEST-TROSY HNCOCACBsample_2isotropicsample_conditions_1
3D BEST-TROSY HNCACBsample_2isotropicsample_conditions_1
3D BEST-TROSY HN(CA)NNHsample_2isotropicsample_conditions_1
3D TROSY HN(COCA)NNHsample_2isotropicsample_conditions_1

Software:

TOPSPIN v1.3 and 2.1, Bruker Biospin - collection

SPARKY, Goddard - data analysis, peak picking

CcpNMR, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 900 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks